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Mouse Anti-EGF/FITC Conjugated antibody
background:
Epidermal growth factor (EGF) is an acid- and heat-stable 53 amino acid protein originally found in rodents and humans. It has been shown to be a potent mitogen for a variety of cell types both in vivo and in vitro. EGF binds to the EGF receptor on the surface of cells and mediates intrinsic phosphorylation of the receptor on tyrosine residues. It has been detected in nearly all body fluids, such as urine (urogastrone), saliva, milk and platelet-rich plasma. EGF, TGF?and vaccinia virus growth factor exhibit 30-40% amino acid homology. Several additional members of the EGF/TGF family have been described; these include Cripto, Amphiregulin and the heparin-binding EGF-like growth factor. Amphiregulin and the heparin-binding EGF-like growth factor both bind to the EGF receptor.
Function:
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6.
Subunit:
Interacts with EGFR and promotes EGFR dimerization. Interacts with RHBDF2. Interacts with RHBDF1; may retain EGF in the endoplasmic reticulum and regulates its degradation through the endoplasmic reticulum-associated degradation (ERAD).
Subcellular Location:
Membrane.
Tissue Specificity:
Expressed in kidney, salivary gland, cerebrum and prostate.
Post-translational modifications:
Phosphorylation at Ser-695 is partial and occurs only if Thr-693 is phosphorylated. Phosphorylation at Thr-678 and Thr-693 by PRKD1 inhibits EGF-induced MAPK8/JNK1 activation. Dephosphorylation by PTPRJ prevents endocytosis and stabilizes the receptor at the plasma membrane. Autophosphorylation at Tyr-1197 is stimulated by methylation at Arg-1199 and enhances interaction with PTPN6. Autophosphorylation at Tyr-1092 and/or Tyr-1110 recruits STAT3.
Monoubiquitinated and polyubiquitinated upon EGF stimulation; which does not affect tyrosine kinase activity or signaling capacity but may play a role in lysosomal targeting. Polyubiquitin linkage is mainly through 'Lys-63', but linkage through 'Lys-48', 'Lys-11' and 'Lys-29' also occur. Deubiquitinated by OTUD7B, preventing degradation.
Methylated. Methylation at Arg-1199 by PRMT5 positively stimulates phosphorylation at Tyr-1197.
DISEASE:
Defects in EGF are the cause of hypomagnesemia type 4 (HOMG4) [MIM:611718]; also known as renal hypomagnesemia normocalciuric. HOMG4 is a disorder characterized by massive renal hypomagnesemia and normal levels of serum calcium and calcium excretion. Clinical features include seizures, mild-to mederate psychomotor retardation, and brisk tendon reflexes.
Similarity:
Contains 9 EGF-like domains.
Contains 9 LDL-receptor class B repeats.
Database links:
Entrez Gene: 13645 Mouse
Entrez Gene: 1950 Human
Omim: 131530 Human
SwissProt: P01133 Human
SwissProt: P01132 Mouse
Unigene: 419815 Human
Unigene: 252481 Mouse
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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